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  • 1
    Publication Date: 1991-09-20
    Description: Neutral sodium emissions encircling Jupiter exhibit an intricate and variable structure that is well matched by a simple loss process from Io's atmosphere. These observations imply that fast neutral sodium is created locally in the Io plasma torus, both near Io and as much as 8 hours downstream. Sodium-bearing molecules may be present in Io's upper atmosphere, where they are ionized by the plasma torus and swept downstream. The molecular ions dissociate and dissociatively recombine on a short time scale, releasing neutral fragments into escape trajectories from Jupiter. This theory explains a diverse set of sodium observations, and it implies that molecular reactions (particularly electron impact ionization and dissociation) are important at the top of Io's atmosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schneider, N M -- Trauger, J T -- Wilson, J K -- Brown, D I -- Evans, R W -- Shemansky, D E -- New York, N.Y. -- Science. 1991 Sep 20;253(5026):1394-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17793479" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2012-02-14
    Description: Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are how human transferrin is specifically targeted, and how the bacteria liberate iron from transferrin at neutral pH. To address these questions, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small-angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292680/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3292680/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noinaj, Nicholas -- Easley, Nicole C -- Oke, Muse -- Mizuno, Naoko -- Gumbart, James -- Boura, Evzen -- Steere, Ashley N -- Zak, Olga -- Aisen, Philip -- Tajkhorshid, Emad -- Evans, Robert W -- Gorringe, Andrew R -- Mason, Anne B -- Steven, Alasdair C -- Buchanan, Susan K -- P41 RR005969/RR/NCRR NIH HHS/ -- P41-RR05969/RR/NCRR NIH HHS/ -- R01 GM086749/GM/NIGMS NIH HHS/ -- R01-DK21739/DK/NIDDK NIH HHS/ -- R01-GM086749/GM/NIGMS NIH HHS/ -- U54 GM087519/GM/NIGMS NIH HHS/ -- U54-GM087519/GM/NIGMS NIH HHS/ -- ZIA DK036143-04/Intramural NIH HHS/ -- England -- Nature. 2012 Feb 12;483(7387):53-8. doi: 10.1038/nature10823.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health, Bethesda, Maryland 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22327295" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoproteins/chemistry/metabolism ; Bacterial Proteins/*chemistry/metabolism/ultrastructure ; Binding Sites ; Biological Transport ; Cattle ; Crystallography, X-Ray ; Humans ; Iron/*metabolism ; Mice ; Models, Molecular ; Molecular Dynamics Simulation ; Neisseria/*metabolism/pathogenicity ; Protein Conformation ; Scattering, Small Angle ; Species Specificity ; Structure-Activity Relationship ; Transferrin/chemistry/metabolism/ultrastructure ; Transferrin-Binding Protein A/*chemistry/*metabolism/ultrastructure ; Transferrin-Binding Protein B/*chemistry/*metabolism/ultrastructure ; X-Ray Diffraction
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 2016-10-01
    Description: We present an empirical model of the energetic electron environment in Jupiter's magnetosphere that we have named the Galileo Interim Radiation Electron Model version-2 (GIRE2) since it is based on Galileo data from the Energetic Particle Detector (EPD). Inside 8 R J , GIRE2 adopts the previously existing model of Divine and Garrett because this region was well sampled by the Pioneer and Voyager spacecraft but poorly covered by Galileo. Outside of 8 R J , the model is based on 10-minute averages of Galileo EPD data as well as on measurements from the Geiger Tube Telescope onboard the Pioneer spacecraft. In the inner magnetosphere the field configuration is dipolar while in the outer magnetosphere it presents a disk-like structure. The gradual transition between these two behaviors is centered at about 17 R J . GIRE2 distinguishes between the two different regions characterized by these two magnetic field topologies. Specifically, GIRE2 consists of an inner trapped omnidirectional model between 8 to 17 R J that smoothly joins onto the original Divine and Garrett model inside 8 R J and onto a GIRE2 plasma sheet model at large radial distances. The model provides a complete picture of the high-energy electron environment in the Jovian magnetosphere from ∼1 to 50 R J . The present manuscript describes in great detail the data sets, formulation, and fittings used in the model and provides a discussion of the predicted high-energy electron fluxes as a function of energy and radial distance from the planet.
    Print ISSN: 0148-0227
    Topics: Geosciences , Physics
    Published by Wiley on behalf of American Geophysical Union (AGU).
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1981-09-25
    Description: Total concentrations of estrogen receptor in the uterine nuclear fraction are reduced rapidly after progesterone treatment of the proestrous hamster. Progesterone acts selectively on the occupied form of the nuclear estrogen receptor, with no effect on the concentration of an unoccupied form. This observation indicates that progesterone modulates the action of estrogen by controlling nuclear retention of the estrogen-receptor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Okulicz, W C -- Evans, R W -- Leavitt, W W -- New York, N.Y. -- Science. 1981 Sep 25;213(4515):1503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7280669" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Cricetinae ; Cytosol/metabolism ; Estradiol/metabolism ; Female ; Progesterone/*pharmacology ; Receptors, Estrogen/*drug effects/metabolism ; Uterus/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1983-10-21
    Description: In the report "Pregnancy interception with a combination of prostaglandins: Studies in monkeys: by J. W. Wilks (30 Sept., p. 1407), figures 2 and 3 on page 1408 were interchanged.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, R W -- New York, N.Y. -- Science. 1983 Oct 21;222(4621):234.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6623074" target="_blank"〉PubMed〈/a〉
    Keywords: Costs and Cost Analysis ; Cyclosporins/therapeutic use ; *Federal Government ; Resource Allocation ; *Transplantation, Homologous/methods
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2013-01-30
    Description: Fluid flow through a two-dimensional fracture network has been simulated using a discrete fracture model. The computed field-scale permeabilities were then compared to those obtained using an equivalent continuum approach in which the permeability of each grid block is first obtained by performing fine-scale simulations of flow through the fracture network within that region. In the equivalent continuum simulations, different grid-sizes were used, corresponding to N by N grids with N = 10, 40, 100 and 400. The field-scale permeabilities found from the equivalent continuum simulations were generally within 10% of the values found from the discrete fracture simulations. The discrepancies between the two approaches seemed to be randomly related to the grid size, as no convergence was observed as N increased. An interesting finding was that the equivalent continuum approach gave accurate results in cases where the grid block size was clearly smaller than the ‘representative elementary volume’.
    Print ISSN: 0026-461X
    Electronic ISSN: 1471-8022
    Topics: Geosciences
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  • 7
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The molecular structure of an iron-containing 18 kDa fragment of duck ovotransferrin, obtained by proteolysis of the intact protein, has been elucidated by protein crystallographic techniques at 2.3 Å resolution. This structure supports a mechanism of iron uptake in the intact protein whereby the binding of the synergistic (bi)carbonate anion is followed by binding of the metal with the lobe in the open configuration. These stages are then followed by domain closure in which the aspartic acid residue plays a further key role, by forming an interdomain hydrogen-bond interaction in addition to serving as a ligand to the iron. This essential dual role is highlighted by model building studies on the C-terminal lobe of a known human variant. In this variant a mutation of a glycine by an arginine residue enables the aspartic acid to form an ion pair and reduce its effectiveness for both metal binding and domain closure. The X-ray structure of the 18 kDa fragment strongly suggests that the histidine residue present at the iron binding site of the intact protein and arising from the second interdomain connecting strand has been removed during the preparative proteolysis.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 71 (2000), S. 4119-4126 
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: The design, construction and operation of a tomographic imaging system on the Compact Toroid Injection Experiment is described. The system measures the total radiated power over energies from visible light up into the extreme ultraviolet. It then reconstructs two dimensional profiles from the data. The reconstruction routine is based on a method known as second order regularization which finds a compromise between smoothness and fit to the data. This method was found to have the best overall fidelity to test images. The hardware and overall reconstruction were calibrated using two different sources. First results from the system under real experimental conditions are presented. © 2000 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 79 (2001), S. 1237-1239 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A compact toroid inductively stores the energy released by a capacitor bank as it is being accelerated. This energy can be stored for a period of more than ten microseconds and then transferred to a load on a much shorter time scale. This article presents framing camera images of the radial compression of plasma trailing behind a compact toroid as the compact toroid leaves its inner electrode. This compression illustrates the basic principles of a compact toroid plasma opening switch which could be used to drive fast z pinches. © 2001 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 98 (1934), S. 287-291 
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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